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Crystal structure of the molybdopterin biosynthesis enzyme moab (TTHA0341) from thermus theromophilus HB8
Analyse Crystal structure of the molybdopterin biosynthesis enzyme moab (TTHA0341) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IS8
- Type
- protein
- Length
- 479 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molybdopterin biosynthesis enzyme, moab
- UniProt
- Q5SLF2
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Molybdopterin biosynthesis enzyme, moab | protein | 159 | 43% helix, 21% strand | Q5SLF2 |
| B | Molybdopterin biosynthesis enzyme, moab | protein | 161 | 42% helix, 21% strand | Q5SLF2 |
Ligands and binding sites
- FMT · Formic acid · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 493 | 0.72 | 0.81 | 43 | empty |
| 2 | 298 | 0.54 | 0.75 | 38 | FMT |
| 3 | 294 | 0.54 | 0.75 | 42 | empty |
| 4 | 282 | 0.52 | 0.74 | 38 | FMT |
| 5 | 86 | 0.52 | 0.84 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–B · 788 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 788 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 637 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2IS8 · Crystal structure of the Molybdopterin biosynthesis enzyme MoaB (TTHA0341) from thermus… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q5SLF2
- Elsewhere: RCSB PDB 2IS8 · PDBe 2IS8 · UniProt Q5SLF2
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